메뉴 건너뛰기




Volumn 25, Issue 9, 2008, Pages 2031-2041

Halogenase genes in nonribosomal peptide synthetase gene clusters of Microcystis (Cyanobacteria): Sporadic distribution and evolution

Author keywords

Aeruginosin; Chlorination; Cyanopeptolin; DNA rearrangement; Halogenase; Internal transcribed spacer; Phylogeny; Secondary peptide metabolite

Indexed keywords

AERUGINOSIN; BACTERIAL ENZYME; CYANOPEPTOLIN; HALOGENASE; PEPTIDE SYNTHASE;

EID: 49749108516     PISSN: 07374038     EISSN: 15371719     Source Type: Journal    
DOI: 10.1093/molbev/msn150     Document Type: Article
Times cited : (58)

References (49)
  • 1
    • 0033609787 scopus 로고    scopus 로고
    • Inhibitors of serine proteases from a waterbloom of the cyanobacterium Microcystis sp
    • Banker R, Carmeli S. 1999. Inhibitors of serine proteases from a waterbloom of the cyanobacterium Microcystis sp. Tetrahedron. 55:10835-10844.
    • (1999) Tetrahedron , vol.55 , pp. 10835-10844
    • Banker, R.1    Carmeli, S.2
  • 2
    • 33644860874 scopus 로고    scopus 로고
    • Transposons inactivate biosynthesis of the nonribosomal peptide microcystin in naturally occurring Planktothrix spp
    • Christiansen G, Kurmayer R, Liu Q, Börner T. 2006. Transposons inactivate biosynthesis of the nonribosomal peptide microcystin in naturally occurring Planktothrix spp. Appl Environ Microbiol. 72:117-123.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 117-123
    • Christiansen, G.1    Kurmayer, R.2    Liu, Q.3    Börner, T.4
  • 3
    • 33644942122 scopus 로고    scopus 로고
    • Identification of peptide metabolites of Microcystis (Cyanobacteria) that inhibit trypsin-like activity in planktonic herbivorous Daphnia (Cladocera)
    • Czarnecki O, Lippert I, Henning M, Welker M. 2006. Identification of peptide metabolites of Microcystis (Cyanobacteria) that inhibit trypsin-like activity in planktonic herbivorous Daphnia (Cladocera). Environ Microbiol. 8:77-87.
    • (2006) Environ Microbiol , vol.8 , pp. 77-87
    • Czarnecki, O.1    Lippert, I.2    Henning, M.3    Welker, M.4
  • 4
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • Dayhoff MO, editor, Washington DC, National Biomedical Research Foundation
    • Dayhoff MO, Schwartz RM, Orcutt BC. 1978. A model of evolutionary change in proteins. In: Dayhoff MO, editor. Atlas of protein sequence structure. Vol. 5. 345-352. Washington (DC): National Biomedical Research Foundation.
    • (1978) Atlas of protein sequence structure , vol.5 , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 5
    • 25844517049 scopus 로고    scopus 로고
    • Tryptophan 7-halogenase (PrnA) structure suggests a mechanism of regioselective chlorination
    • Dong C, Flecks S, Unversucht S, Haupt C, van Pée KH, Naismith JH. 2005. Tryptophan 7-halogenase (PrnA) structure suggests a mechanism of regioselective chlorination. Science. 309:2216-2219.
    • (2005) Science , vol.309 , pp. 2216-2219
    • Dong, C.1    Flecks, S.2    Unversucht, S.3    Haupt, C.4    van Pée, K.H.5    Naismith, J.H.6
  • 6
    • 25444465451 scopus 로고    scopus 로고
    • Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis
    • Dorrestein PC, Yeh E, Garneau-Tsodikova S, Kelleher NL, Walsh CT. 2005. Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis. Proc Natl Acad Sci USA. 102:13843-13848.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13843-13848
    • Dorrestein, P.C.1    Yeh, E.2    Garneau-Tsodikova, S.3    Kelleher, N.L.4    Walsh, C.T.5
  • 7
    • 0037350329 scopus 로고    scopus 로고
    • Clorobiocin biosynthesis in Streptomyces: Identification of the halogenase and generation of structural analogs
    • Eustáquio AS, Gust B, Luft T, Li SM, Chater KF, Heide L. 2003. Clorobiocin biosynthesis in Streptomyces: identification of the halogenase and generation of structural analogs. Chem Biol. 10:279-288.
    • (2003) Chem Biol , vol.10 , pp. 279-288
    • Eustáquio, A.S.1    Gust, B.2    Luft, T.3    Li, S.M.4    Chater, K.F.5    Heide, L.6
  • 8
    • 46649118468 scopus 로고    scopus 로고
    • Frangeul L, Quillardet P, Castets AM, et al. (20 co-authors). 2008. Highly plastic genome of Microcystis aeruginosa PCC7806, an ubiquitous toxic freshwater cyanobacterium. BMC Genomics. 9:274.
    • Frangeul L, Quillardet P, Castets AM, et al. (20 co-authors). 2008. Highly plastic genome of Microcystis aeruginosa PCC7806, an ubiquitous toxic freshwater cyanobacterium. BMC Genomics. 9:274.
  • 9
    • 33645461070 scopus 로고    scopus 로고
    • Halogenation of unactivated carbon centers in natural product biosynthesis: Trichlorination of leucine during barbamide biosynthesis
    • Galonic DP, Vaillancourt FH, Walsh CT. 2006. Halogenation of unactivated carbon centers in natural product biosynthesis: trichlorination of leucine during barbamide biosynthesis. J Am Chem Soc. 128:3900-3901.
    • (2006) J Am Chem Soc , vol.128 , pp. 3900-3901
    • Galonic, D.P.1    Vaillancourt, F.H.2    Walsh, C.T.3
  • 10
    • 14144255529 scopus 로고    scopus 로고
    • Molecular phylogeny of Vipera Laurenti, 1768 and the related genera Macrovipera (Reuss, 1927) and Daboia (Gray, 1842), with comments about neurotoxic Vipera aspis aspis populations
    • Garrigues T, Dauga C, Ferquel E, Choumet V, Failloux AB. 2005. Molecular phylogeny of Vipera Laurenti, 1768 and the related genera Macrovipera (Reuss, 1927) and Daboia (Gray, 1842), with comments about neurotoxic Vipera aspis aspis populations. Mol Phylogenet Evol. 35:35-47.
    • (2005) Mol Phylogenet Evol , vol.35 , pp. 35-47
    • Garrigues, T.1    Dauga, C.2    Ferquel, E.3    Choumet, V.4    Failloux, A.B.5
  • 11
    • 0030807655 scopus 로고    scopus 로고
    • BIONJ: An improved version of the NJ algorithm based on a simple model of sequence data
    • Gascuel O. 1997. BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data. Mol Biol Evol. 14:685-695.
    • (1997) Mol Biol Evol , vol.14 , pp. 685-695
    • Gascuel, O.1
  • 12
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate phylogenies by maximum likelihood
    • Guindon S, Gascuel O. 2003. A simple, fast, and accurate algorithm to estimate phylogenies by maximum likelihood. Syst Biol. 52:696-704.
    • (2003) Syst Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 13
    • 0022346887 scopus 로고
    • The role of the chlorine substituents in the antibiotic vancomycin: Preparation and characterization of mono- and didechlorovancomycin
    • Harris CM, Kannan R, Kopecka H, Harris TM. 1985. The role of the chlorine substituents in the antibiotic vancomycin: preparation and characterization of mono- and didechlorovancomycin. J Am Chem Soc. 107:6652-6658.
    • (1985) J Am Chem Soc , vol.107 , pp. 6652-6658
    • Harris, C.M.1    Kannan, R.2    Kopecka, H.3    Harris, T.M.4
  • 14
    • 34248579751 scopus 로고    scopus 로고
    • Biosynthetic pathway and structure analysis of aeruginoside 126A and B, cyanobacterialpeptides bearing an unusual 2-carboxy-6-hydroxyoctaindole moiety
    • Ishida K, Christiansen G, Yoshida WY, Welker M, Bonjoch J, Hertweck C, Börner T, Hemscheidt TK, Dittmann E. 2007. Biosynthetic pathway and structure analysis of aeruginoside 126A and B, cyanobacterialpeptides bearing an unusual 2-carboxy-6-hydroxyoctaindole moiety. Chem Biol. 14:565-576.
    • (2007) Chem Biol , vol.14 , pp. 565-576
    • Ishida, K.1    Christiansen, G.2    Yoshida, W.Y.3    Welker, M.4    Bonjoch, J.5    Hertweck, C.6    Börner, T.7    Hemscheidt, T.K.8    Dittmann, E.9
  • 15
    • 0032578683 scopus 로고    scopus 로고
    • Four new microginins, linear peptides from the cyanobacterium Microcystis aeruginosa
    • Ishida K, Matsuda H, Murakami M. 1998. Four new microginins, linear peptides from the cyanobacterium Microcystis aeruginosa. Tetrahedron. 54:13475-13484.
    • (1998) Tetrahedron , vol.54 , pp. 13475-13484
    • Ishida, K.1    Matsuda, H.2    Murakami, M.3
  • 16
    • 0033520230 scopus 로고    scopus 로고
    • Aeruginosins, protease inhibitors from the cyanobacterium Microcystis aeruginosa
    • Ishida K, Okita Y, Matsuda H, Okino T, Murakami M. 1999. Aeruginosins, protease inhibitors from the cyanobacterium Microcystis aeruginosa. Tetrahedron. 55:10971-10988.
    • (1999) Tetrahedron , vol.55 , pp. 10971-10988
    • Ishida, K.1    Okita, Y.2    Matsuda, H.3    Okino, T.4    Murakami, M.5
  • 17
    • 0034129537 scopus 로고    scopus 로고
    • Comparison of conserved structural and regulatory domains within divergent 16S rRNA-23S rRNA spacer sequences of cyanobacteria
    • Iteman I, Rippka R, Tandeau de Marsac N, Herdman M. 2000. Comparison of conserved structural and regulatory domains within divergent 16S rRNA-23S rRNA spacer sequences of cyanobacteria. Microbiol SGM. 146:1275-1286.
    • (2000) Microbiol SGM , vol.146 , pp. 1275-1286
    • Iteman, I.1    Rippka, R.2    Tandeau de Marsac, N.3    Herdman, M.4
  • 19
    • 36849010759 scopus 로고    scopus 로고
    • Novel insights into evolution of protistan polyketide synthases through phylogenomic analysis
    • John U, Beszteri B, Derelle E, van de Peer Y, Read B, Moreau H, Cembella AD. 2008. Novel insights into evolution of protistan polyketide synthases through phylogenomic analysis. Protist. 159:21-30.
    • (2008) Protist , vol.159 , pp. 21-30
    • John, U.1    Beszteri, B.2    Derelle, E.3    van de Peer, Y.4    Read, B.5    Moreau, H.6    Cembella, A.D.7
  • 20
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM. 1992. The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci. 8:275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 21
    • 40949129063 scopus 로고    scopus 로고
    • Kaneko T, Nakajima N, Okamoto S, et al. (23 co-authors). 2007. Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843. DNA Res. 14:247-256.
    • Kaneko T, Nakajima N, Okamoto S, et al. (23 co-authors). 2007. Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843. DNA Res. 14:247-256.
  • 22
    • 0034600905 scopus 로고    scopus 로고
    • Purification and partial characterization of tryptophan 7-halogenase (PrnA) from Pseudomonas fluorescens
    • Keller S, Wage T, Hohaus K, Hölzer M, Eichhorn E, van Pée KH. 2000. Purification and partial characterization of tryptophan 7-halogenase (PrnA) from Pseudomonas fluorescens. Angew Chem Int Ed Engl. 39:2300-2302.
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 2300-2302
    • Keller, S.1    Wage, T.2    Hohaus, K.3    Hölzer, M.4    Eichhorn, E.5    van Pée, K.H.6
  • 23
    • 12344269158 scopus 로고    scopus 로고
    • Different versions of the Dayhoff rate matrix
    • Kosiol C, Goldman N. 2005. Different versions of the Dayhoff rate matrix. Mol Biol Evol. 22:193-199.
    • (2005) Mol Biol Evol , vol.22 , pp. 193-199
    • Kosiol, C.1    Goldman, N.2
  • 24
    • 0028518887 scopus 로고
    • Atomic structure of the trypsin-A90720A complex: A unified approach to structure and function
    • Lee AY, Smitka TA, Bonjouklian R, Clardy J. 1994. Atomic structure of the trypsin-A90720A complex: a unified approach to structure and function. Chem Biol. 1:113-117.
    • (1994) Chem Biol , vol.1 , pp. 113-117
    • Lee, A.Y.1    Smitka, T.A.2    Bonjouklian, R.3    Clardy, J.4
  • 25
    • 0023256559 scopus 로고
    • Slipped-strand mispairing: A major mechanism for DNA sequence evolution
    • Levinson G, Gutman GA. 1987. Slipped-strand mispairing: a major mechanism for DNA sequence evolution. Mol Biol Evol. 4:203-221.
    • (1987) Mol Biol Evol , vol.4 , pp. 203-221
    • Levinson, G.1    Gutman, G.A.2
  • 27
    • 17244367035 scopus 로고    scopus 로고
    • Variability of mcy-genes in the genus Planktothrix (Oscillatoriales, Cyanobacteria)
    • Mbedi S, Welker M, Fastner J, Wiedner C. 2005. Variability of mcy-genes in the genus Planktothrix (Oscillatoriales, Cyanobacteria). FEMS Microbiol Lett. 245:299-306.
    • (2005) FEMS Microbiol Lett , vol.245 , pp. 299-306
    • Mbedi, S.1    Welker, M.2    Fastner, J.3    Wiedner, C.4
  • 28
    • 0242417422 scopus 로고    scopus 로고
    • Natural variation in the microcystin synthetase operon mcyABC and impact on microcystin production in Microcystis strains
    • Mikalsen B, Boison G, Skulberg OM, Fastner J, Davies W, Gabrielsen TM, Rudi K, Jakobsen KS. 2003. Natural variation in the microcystin synthetase operon mcyABC and impact on microcystin production in Microcystis strains. J Bacteriol. 185:2774-2785.
    • (2003) J Bacteriol , vol.185 , pp. 2774-2785
    • Mikalsen, B.1    Boison, G.2    Skulberg, O.M.3    Fastner, J.4    Davies, W.5    Gabrielsen, T.M.6    Rudi, K.7    Jakobsen, K.S.8
  • 33
    • 0033926435 scopus 로고    scopus 로고
    • Rouhiainen L, Paulin L, Suomalainen S, Hyytiainen H, Buikema W, Haselkorn R, Sivonen K. 2000. Genes encoding synthetases of cyclic depsipeptides, anabaenopeptilides, in Anabaena strain 90. Mol Microbiol. 37:156-167.
    • Rouhiainen L, Paulin L, Suomalainen S, Hyytiainen H, Buikema W, Haselkorn R, Sivonen K. 2000. Genes encoding synthetases of cyclic depsipeptides, anabaenopeptilides, in Anabaena strain 90. Mol Microbiol. 37:156-167.
  • 34
    • 36649038371 scopus 로고    scopus 로고
    • Comparison of cyanopeptolin genes in Planktothrix, Microcystis, and Anabaena strains: Evidence for independent evolution within each genus
    • Rounge TB, Rohrlack T, Tooming-Klunderud A, Kristensen T, Jakobsen KS. 2007. Comparison of cyanopeptolin genes in Planktothrix, Microcystis, and Anabaena strains: evidence for independent evolution within each genus. Appl Environ Microbiol. 73:7322-7330.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 7322-7330
    • Rounge, T.B.1    Rohrlack, T.2    Tooming-Klunderud, A.3    Kristensen, T.4    Jakobsen, K.S.5
  • 35
    • 0030894360 scopus 로고    scopus 로고
    • Aeruginosins 205A and -B, serine protease inhibitory glycopeptides from the cyanobacterium Oscillatoria agardhii (NIES-205)
    • Shin HJ, Matsuda H, Murakami M, Yamaguchi K. 1997. Aeruginosins 205A and -B, serine protease inhibitory glycopeptides from the cyanobacterium Oscillatoria agardhii (NIES-205). J Org Chem. 62:1810-1813.
    • (1997) J Org Chem , vol.62 , pp. 1810-1813
    • Shin, H.J.1    Matsuda, H.2    Murakami, M.3    Yamaguchi, K.4
  • 36
    • 0034634643 scopus 로고    scopus 로고
    • Biosynthetic pathway and origin of the chlorinated methyl group in barbamide and dechlorobarbamide, metabolites from the marine cyanobacterium Lyngbya majuscula
    • Sitachitta N, Marquez BL, Williamson RT, Rossi J, Roberts MA, Gerwick WH, Nguyen V-A, Willis CL. 2000. Biosynthetic pathway and origin of the chlorinated methyl group in barbamide and dechlorobarbamide, metabolites from the marine cyanobacterium Lyngbya majuscula. Tetrahedron. 56:9103-9113.
    • (2000) Tetrahedron , vol.56 , pp. 9103-9113
    • Sitachitta, N.1    Marquez, B.L.2    Williamson, R.T.3    Rossi, J.4    Roberts, M.A.5    Gerwick, W.H.6    Nguyen, V.-A.7    Willis, C.L.8
  • 37
    • 2942665460 scopus 로고    scopus 로고
    • Evidence for recombination in the microcystin synthetase (mcy) genes of toxic cyanobacteria Microcystis spp
    • Tanabe Y, Kaya K, Watanabe MM. 2004. Evidence for recombination in the microcystin synthetase (mcy) genes of toxic cyanobacteria Microcystis spp. Mol Evol. 58:633-641.
    • (2004) Mol Evol , vol.58 , pp. 633-641
    • Tanabe, Y.1    Kaya, K.2    Watanabe, M.M.3
  • 38
    • 34249090193 scopus 로고    scopus 로고
    • Structural analysis of a non-ribosomal halogenated cyclic peptide and its putative operon from Microcystis: Implications for evolution of cyanopeptolins
    • Tooming-Klunderud A, Rohrlack T, Shalchian-Tabrizi K, Kristensen T, Jakobsen KS. 2007. Structural analysis of a non-ribosomal halogenated cyclic peptide and its putative operon from Microcystis: implications for evolution of cyanopeptolins. Microbiol SGM. 153:1382-1393.
    • (2007) Microbiol SGM , vol.153 , pp. 1382-1393
    • Tooming-Klunderud, A.1    Rohrlack, T.2    Shalchian-Tabrizi, K.3    Kristensen, T.4    Jakobsen, K.S.5
  • 40
    • 22544479980 scopus 로고    scopus 로고
    • SyrB2 in syringomycin E biosynthesis is a nonheme FeII α-ketoglutarate- and O2-dependent halogenase
    • Vaillancourt FH, Yin J, Walsh CT. 2005. SyrB2 in syringomycin E biosynthesis is a nonheme FeII α-ketoglutarate- and O2-dependent halogenase. Proc Natl Acad Sci USA. 102:10111-10116.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10111-10116
    • Vaillancourt, F.H.1    Yin, J.2    Walsh, C.T.3
  • 41
    • 33646816419 scopus 로고    scopus 로고
    • Flavin-dependent halogenases involved in secondary metabolism in bacteria
    • van Pée KH, Patallo EP. 2006. Flavin-dependent halogenases involved in secondary metabolism in bacteria. Appl Microbiol Biotechnol. 70:631-641.
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 631-641
    • van Pée, K.H.1    Patallo, E.P.2
  • 42
    • 84983210879 scopus 로고    scopus 로고
    • Enzymology and molecular genetics of biological halogenation
    • Gribble GW, editor, Berlin Germany, Springer. p
    • van Pée KH, Zehner S. 2003. Enzymology and molecular genetics of biological halogenation. In: Gribble GW, editor. Natural production of organohalogen compounds. Berlin (Germany): Springer. p. 171-199.
    • (2003) Natural production of organohalogen compounds , pp. 171-199
    • van Pée, K.H.1    Zehner, S.2
  • 43
    • 27144531769 scopus 로고    scopus 로고
    • Cyanopeptolin 954, a chlorine-containing chymotrypsin inhibitor of Microcystis aeruginosa NIVA Cya 43
    • von Elert E, Oberer L, Merkel P, Huhn T, Blom JF. 2005. Cyanopeptolin 954, a chlorine-containing chymotrypsin inhibitor of Microcystis aeruginosa NIVA Cya 43. J Nat Prod. 68:1324-1327.
    • (2005) J Nat Prod , vol.68 , pp. 1324-1327
    • von Elert, E.1    Oberer, L.2    Merkel, P.3    Huhn, T.4    Blom, J.F.5
  • 44
    • 3142757234 scopus 로고    scopus 로고
    • Diversity and distribution of Microcystis (Cyanobacteria) oligopeptide chemotypes from natural communities studied by single colony mass spectrometry
    • Welker M, Brunke M, Preussel K, Lippert I, von Döhren H. 2004. Diversity and distribution of Microcystis (Cyanobacteria) oligopeptide chemotypes from natural communities studied by single colony mass spectrometry. Microbiol SGM. 150:1785-1796.
    • (2004) Microbiol SGM , vol.150 , pp. 1785-1796
    • Welker, M.1    Brunke, M.2    Preussel, K.3    Lippert, I.4    von Döhren, H.5
  • 45
    • 33746924528 scopus 로고    scopus 로고
    • Detection and identification of oligopeptides in Microcystis (cyanobacteria) colonies: Toward an understanding of metabolic diversity
    • Welker M, Marsalek B, Sejnohova L, von Döhren H. 2006. Detection and identification of oligopeptides in Microcystis (cyanobacteria) colonies: toward an understanding of metabolic diversity. Peptides. 27:2090-2103.
    • (2006) Peptides , vol.27 , pp. 2090-2103
    • Welker, M.1    Marsalek, B.2    Sejnohova, L.3    von Döhren, H.4
  • 46
    • 33744965454 scopus 로고    scopus 로고
    • Cyanobacterial peptides - nature's own combinatorial biosynthesis
    • Welker M, von Döhren H. 2006. Cyanobacterial peptides - nature's own combinatorial biosynthesis. FEMS Microbiol Rev. 30:530-563.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 530-563
    • Welker, M.1    von Döhren, H.2
  • 47
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S, Goldman N. 2001. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol Biol Evol. 18:691-699.
    • (2001) Mol Biol Evol , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 48
    • 4143127694 scopus 로고    scopus 로고
    • A novel halogenase gene from the pentachloropseudilin producer Actinoplanes sp. ATCC 33002 and detection of in vitro halogenase activity
    • Wynands I, van Pée KH. 2004. A novel halogenase gene from the pentachloropseudilin producer Actinoplanes sp. ATCC 33002 and detection of in vitro halogenase activity. FEMS Microbiol Lett. 237:363-367.
    • (2004) FEMS Microbiol Lett , vol.237 , pp. 363-367
    • Wynands, I.1    van Pée, K.H.2
  • 49
    • 15244349569 scopus 로고    scopus 로고
    • Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis
    • Yeh E, Garneau S, Walsh CT. 2005. Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis. Proc Natl Acad Sci USA. 102:3960-3965.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3960-3965
    • Yeh, E.1    Garneau, S.2    Walsh, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.